The interaction of concanavalin A with sheep erythrocytes

Autor: Virgie G. Shore, Bernard Shore
Rok vydání: 1974
Předmět:
Zdroj: Biochimica et biophysica acta. 373(2)
ISSN: 0006-3002
Popis: Concanavalin A and 125 I-labelled concanavalin A were used as probes for comparison of sheep low-potassium (LK) and high-potassium (HK) erythrocytes with respect to their agglutinability and membrane properties. Under conditions of equivalent concanavalin A binding, freshly isolated sheep HK cells agglutinated to a much greater extent than the LK cells at 23 or 35 °C; agglutination was progressive over periods of 1–4 h, but the differential between LK and HK cells persisted. On additional standing overnight in the cold, both LK and HK cells were extensively agglutinated. After preincubation in a salt-buffer solution (without lectin) for 4 h at 35 °C followed by standing overnight at 4 °C, rapid extensive agglutination but not increased binding of concanavalin A occured in both sheep HK and LK cells. Cells preincubated in the presence of an energy source and/or bovine plasma albumin also agglutinated rapidly. The rate of agglutination of freshly isolated cells of either kind was not decreased by the presence of an energy supply. Agglutination of sheep LK and HK erythrocytes by concanavalin A appears to proceed by two steps: the first, a relatively rapid and temperature-independent binding of lectin which is very similar if not identical in the LK and HK cells; and the second, agglutination of the cells, which is slow by comparison with dog and rabbit erythrocytes under the same conditions. The second step depends upon a change in the cells that occurs relatively slowly after their isolation whether or not concanavalin A or an energy supply is present. Possibly this change occurs more rapidly in HK cells and thus causes the differential in agglutinability of LK and HK cells.
Databáze: OpenAIRE